1ktw

IOTA-CARRAGEENASE COMPLEXED TO IOTA-CARRAGEENAN FRAGMENTS

spinqualitylabelsall models 1ktw, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ktw is a 2 chain structure with sequence from Alteromonas macleodii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: CA, CL, DGS, G4S, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CGIA_ALTMA Hydrolyzes iota-carrageenans, sulfated 1,3-alpha-1,4-beta galactans from red algal cell walls, with an inversion of anomeric configuration. Also active against hybrid iota-/nu-carrageenan, not active against kappa- or lambda-carrageenans.[UniProtKB:Q9F284] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed iota-Carrageenans are sulfated 1,3-alpha-1,4-beta-galactans from the cell walls of red algae, which auto-associate into crystalline fibers made of aggregates of double-stranded helices. iota-Carrageenases, which constitute family 82 of glycoside hydrolases, fold into a right-handed beta-helix. Here, the structure of Alteromonas fortis iota-carrageenase bound to iota-carrageenan fragments was solved at 2.0A resolution (PDB 1KTW). The enzyme holds a iota-carrageenan tetrasaccharide (subsites +1 to +4) and a disaccharide (subsites -3, -4), thus providing the first direct determination of a 3D structure of iota-carrageenan. Electrostatic interactions between basic protein residues and the sulfate substituents of the polysaccharide chain dominate iota-carrageenan recognition. Glu245 and Asp247 are the proton donor and the base catalyst, respectively. C-terminal domain A, which was highly flexible in the native enzyme structure, adopts a alpha/beta-fold, also found in DNA/RNA-binding domains. In the substrate-enzyme complex, this polyanion-binding module shifts toward the beta-helix groove, forming a tunnel. Thus, from an open conformation which allows for the initial endo-attack of iota-carrageenan chains, the enzyme switches to a closed-tunnel form, consistent with its highly processive character, as seen from the electron-microscopy analysis of the degradation of iota-carrageenan fibers. The structural bases of the processive degradation of iota-carrageenan, a main cell wall polysaccharide of red algae.,Michel G, Helbert W, Kahn R, Dideberg O, Kloareg B J Mol Biol. 2003 Nov 28;334(3):421-33. PMID:14623184 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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